Structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy

Deciphering the mechanism of protein folding is one of the most desirable goals in the field of structural biology. Apart from the structural information about the native state, in-depth knowledge about the conformational properties of the unfolded and intermediate states of proteins is important to...

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Main Author:	Sebanti Gupta
Other Authors:	Surajit Bhattacharyya
Format:	Theses and Dissertations
Language:	English
Published:	2014
Subjects:	DRNTU::Science::Biological sciences
Online Access:	http://hdl.handle.net/10356/60568
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Institution:	Nanyang Technological University
Language:	English

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spelling	sg-ntu-dr.10356-605682023-02-28T18:36:14Z Structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy Sebanti Gupta Surajit Bhattacharyya School of Biological Sciences DRNTU::Science::Biological sciences Deciphering the mechanism of protein folding is one of the most desirable goals in the field of structural biology. Apart from the structural information about the native state, in-depth knowledge about the conformational properties of the unfolded and intermediate states of proteins is important to understand the folding process. This information can further provide insight into the events of protein misfolding and aggregation that result in variety of diseases. Doctor of Philosophy (SBS) 2014-05-28T07:24:22Z 2014-05-28T07:24:22Z 2013 2013 Thesis http://hdl.handle.net/10356/60568 en 252 p. application/pdf
institution	Nanyang Technological University
building	NTU Library
continent	Asia
country	Singapore Singapore
content_provider	NTU Library
collection	DR-NTU
language	English
topic	DRNTU::Science::Biological sciences
spellingShingle	DRNTU::Science::Biological sciences Sebanti Gupta Structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy
description	Deciphering the mechanism of protein folding is one of the most desirable goals in the field of structural biology. Apart from the structural information about the native state, in-depth knowledge about the conformational properties of the unfolded and intermediate states of proteins is important to understand the folding process. This information can further provide insight into the events of protein misfolding and aggregation that result in variety of diseases.
author2	Surajit Bhattacharyya
author_facet	Surajit Bhattacharyya Sebanti Gupta
format	Theses and Dissertations
author	Sebanti Gupta
author_sort	Sebanti Gupta
title	Structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy
title_short	Structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy
title_full	Structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy
title_fullStr	Structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy
title_full_unstemmed	Structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy
title_sort	structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy
publishDate	2014
url	http://hdl.handle.net/10356/60568
_version_	1759854392334352384

Structural and dynamic characterization of the near native and unfolded states of protein interaction domains by nmr spectroscopy

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